Death brings new life to muscle

Yu, Shannon F.; Baylies, Mary K.

doi:10.1038/nature12097

Cited by 11 publications

(13 citation statements)

References 13 publications

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“…However, although BAI1-null animals exhibit a reduction in their ability to repair injured muscle, they do not display major defects in muscle development. These results argue for a specialized function of BAI1 in muscle regeneration and an indirect role in fusion (33,43). Although our work does not rule out that BAI3 could also contribute to muscle regeneration, it highlights the unique ability of this GPCR to mediate primary myoblast fusion during embryonic development.…”

Section: Discussionmentioning

confidence: 71%

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Hamoud

Tran

Croteau

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

100

113

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Muscle fibers form as a result of myoblast fusion, yet the cell surface receptors regulating this process are unknown in vertebrates. In Drosophila, myoblast fusion involves the activation of the Rac pathway by the guanine nucleotide exchange factor Myoblast City and its scaffolding protein ELMO, downstream of cellsurface cell-adhesion receptors. We previously showed that the mammalian ortholog of Myoblast City, DOCK1, functions in an evolutionarily conserved manner to promote myoblast fusion in mice. In search for regulators of myoblast fusion, we identified the G-protein coupled receptor brain-specific angiogenesis inhibitor (BAI3) as a cell surface protein that interacts with ELMO. In cultured cells, BAI3 or ELMO1/2 loss of function severely impaired myoblast fusion without affecting differentiation and cannot be rescued by reexpression of BAI3 mutants deficient in ELMO binding. The related BAI protein family member, BAI1, is functionally distinct from BAI3, because it cannot rescue the myoblast fusion defects caused by the loss of BAI3 function. Finally, embryonic muscle precursor expression of a BAI3 mutant unable to bind ELMO was sufficient to block myoblast fusion in vivo. Collectively, our findings provide a role for BAI3 in the relay of extracellular fusion signals to their intracellular effectors, identifying it as an essential transmembrane protein for embryonic vertebrate myoblast fusion. myotube formation | myogenesis | model system | ced-12 | RhoGTP

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Section: Discussionmentioning

confidence: 71%

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Hamoud

Tran

Croteau

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

100

113

View full text Add to dashboard Cite

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“…Activation of this pathway increases protein synthesis and induces muscle hypertrophy (Taha and Klip 1999 ; Bodine et al. 2001 ; Miyazaki and Esser 2009 ; Yu and Baylies 2013 ) but its activity is attenuated in streptozotocin-induced diabetic animals due to reduced plasma levels of insulin and IGF-1 (Like and Rossini 1976 ; Yang et al. 1990 ).…”

Section: Introductionmentioning

confidence: 99%

Overload-induced skeletal muscle hypertrophy is not impaired in STZ-diabetic rats

et al. 2015

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The aim of this study was to evaluate the effect of overload-induced hypertrophy on extensor digitorum longus (EDL) and soleus muscles of streptozotocin-induced diabetic rats. The overload-induced hypertrophy and absolute tetanic and twitch forces increases in EDL and soleus muscles were not different between diabetic and control rats. Phospho-Akt and rpS6 contents were increased in EDL muscle after 7 days of overload and returned to the pre-overload values after 30 days. In the soleus muscle, the contents of total and phospho-Akt and total rpS6 were increased in both groups after 7 days. The contents of total Akt in controls and total rpS6 and phospho-Akt in the diabetic rats remained increased after 30 days. mRNA expression after 7 days of overload in the EDL muscle of control and diabetic animals showed an increase in MGF and follistatin and a decrease in myostatin and Axin2. The expression of FAK was increased and of MuRF-1 and atrogin-1 decreased only in the control group, whereas Ankrd2 expression was enhanced only in diabetic rats. In the soleus muscle caused similar changes in both groups: increase in FAK and MGF and decrease in Wnt7a, MuRF-1, atrogin-1, and myostatin. Differences between groups were observed only in the increased expression of follistatin in diabetic animals and decreased Ankrd2 expression in the control group. So, insulin deficiency does not impair the overload-induced hypertrophic response in soleus and EDL muscles. However, different mechanisms seem to be involved in the comparable hypertrophic responses of skeletal muscle in control and diabetic animals.

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“…For example, cell surface exposure of PS on myoblasts is an indispensable event for myoblast fusion [60, 61] and treatment with PS liposomes can enhance muscle fibre formation in vitro [62]. Conversely, ablation of the PS receptor has been found to impair muscle regeneration following injury in mice [63, 64]. SM levels also relate to the state of activation of muscle myogenic precursor cells (satellite cells) [65], with SM metabolism to the metabolite sphingosine-1-phosphate (S1P) being a crucial pathway in satellite cell activation/proliferation [66–70], myoblast migration [71] and myogenic differentiation [72–77].…”

Section: Discussionmentioning

confidence: 99%

Dietary supplementation with bovine-derived milk fat globule membrane lipids promotes neuromuscular development in growing rats

et al. 2017

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BackgroundThe milk fat globule membrane (MFGM) is primarily composed of polar phospho- and sphingolipids, which have established biological effects on neuroplasticity. The present study aimed to investigate the effect of dietary MFGM supplementation on the neuromuscular system during post-natal development.MethodsGrowing rats received dietary supplementation with bovine-derived MFGM mixtures consisting of complex milk lipids (CML), beta serum concentrate (BSC) or a complex milk lipid concentrate (CMLc) (which lacks MFGM proteins) from post-natal day 10 to day 70.ResultsSupplementation with MFGM mixtures enriched in polar lipids (BSC and CMLc, but not CML) increased the plasma phosphatidylcholine (PC) concentration, with no effect on plasma phosphatidylinositol (PI), phosphatidylethanolamine (PE), phosphatidylserine (PS) or sphingomyelin (SM). In contrast, muscle PC was reduced in rats receiving supplementation with both BSC and CMLc, whereas muscle PI, PE, PS and SM remained unchanged. Rats receiving BSC and CMLc (but not CML) displayed a slow-to-fast muscle fibre type profile shift (MyHCI → MyHCIIa) that was associated with elevated expression of genes involved in myogenic differentiation (myogenic regulatory factors) and relatively fast fibre type specialisation (Myh2 and Nfatc4). Expression of neuromuscular development genes, including nerve cell markers, components of the synaptogenic agrin–LRP4 pathway and acetylcholine receptor subunits, was also increased in muscle of rats supplemented with BSC and CMLc (but not CML).ConclusionsThese findings demonstrate that dietary supplementation with bovine-derived MFGM mixtures enriched in polar lipids can promote neuromuscular development during post-natal growth in rats, leading to shifts in adult muscle phenotype.Electronic supplementary materialThe online version of this article (doi:10.1186/s12986-017-0161-y) contains supplementary material, which is available to authorized users.

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Death brings new life to muscle

Abstract: Fusion of muscle cells called myoblasts underlies the generation and maintenance of skeletal muscle throughout an animal’s life. Emerging data indicate that cell death acts as a signal to enhance these processes in mammals.

Cited by 11 publications

References 13 publications

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates

Overload-induced skeletal muscle hypertrophy is not impaired in STZ-diabetic rats

Dietary supplementation with bovine-derived milk fat globule membrane lipids promotes neuromuscular development in growing rats

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